Research Article Open Access

Synchrotron Powder Diffraction Study of Radiation Damage in Langmuir Blodgett Nanotemplate Crystallised Protein

Jonathan P. Wright1, Eugenia Pechkova2 and Claudio Nicolini3
  • 1 ESRF, France
  • 2 LNB-DIMES University of Genova, Italy
  • 3 Nanoworld Institute, Italy

Abstract

Polycrystalline samples of lysozyme were prepared with and without a Langmuir-Blodgett (LB) thin film template via both the hanging drop method and batch crystallisation. Powder diffraction methods are used to compare these samples and to measure their resistance to radiation damage at room temperature. The X-ray induced amorphisation of the samples was followed as a function of time and it was shown that diffraction does not entirely disappear even at very long exposure times. Two distinct kinetic timescales are evident suggesting that early and late stage processes are quite different. Radiation damage was also shown to be localized in the sample in the region where the beam impinges.

American Journal of Biochemistry and Biotechnology
Volume 10 No. 3, 2014, 162-168

DOI: https://doi.org/10.3844/ajbbsp.2014.162.168

Submitted On: 17 October 2014 Published On: 12 November 2014

How to Cite: Wright, J. P., Pechkova, E. & Nicolini, C. (2014). Synchrotron Powder Diffraction Study of Radiation Damage in Langmuir Blodgett Nanotemplate Crystallised Protein. American Journal of Biochemistry and Biotechnology, 10(3), 162-168. https://doi.org/10.3844/ajbbsp.2014.162.168

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Keywords

  • Powder Diffraction
  • Lysozyme
  • Synchrotron Radiation